Afamin
Intramolecular
Cysteine 192 and cysteine 201
Cysteine 77 and cysteine 86
Cysteine 536 and cysteine 581
Cysteine 416 and cysteine 462
Cysteine 580 and cysteine 589
Cysteine 302 and cysteine 313
Cysteine 384 and cysteine 393
Cysteine 289 and cysteine 303
Cysteine 99 and cysteine 114
Cysteine 148 and cysteine 193
More...Cysteine 340 and cysteine 385
Cysteine 498 and cysteine 509
Cysteine 113 and cysteine 124
Cysteine 269 and cysteine 277
Cysteine 483 and cysteine 499
Cysteine 461 and cysteine 470
Cysteine 224 and cysteine 270
Cysteine 192 and cysteine 193
Cysteine 302 and cysteine 303
Cysteine 384 and cysteine 385
Cysteine 461 and cysteine 462
Cysteine 113 and cysteine 114
Cysteine 498 and cysteine 499
Cysteine 340 and cysteine 384
Cysteine 269 and cysteine 270
Cysteine 580 and cysteine 581
Cysteine 289 and cysteine 302
Cysteine 99 and cysteine 113
Cysteine 536 and cysteine 580
Cysteine 416 and cysteine 461
Cysteine 385 and cysteine 393
Cysteine 148 and cysteine 192
Cysteine 483 and cysteine 498
Cysteine 193 and cysteine 201
Cysteine 224 and cysteine 269
Cysteine 114 and cysteine 124
Cysteine 536 and cysteine 589
Cysteine 499 and cysteine 509
Cysteine 148 and cysteine 201
Cysteine 581 and cysteine 589
5okl A 171 A 180
A redox-regulated disulphide may form within Afamin between cysteines 192 and 201 (171 and 180 respectively in this structure).
Details
Redox score ?
88
PDB code
5okl
Structure name
human afamin monoclinic crystal form
Structure deposition date
2017-07-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
39
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43652
Residue number A
192
Residue number B
201
Peptide name
Afamin
Ligandability
Cysteine 192 of Afamin
Cysteine 201 of Afamin
5okl A 56 A 65
A redox-regulated disulphide may form within Afamin between cysteines 77 and 86 (56 and 65 respectively in this structure).
Details
Redox score ?
87
PDB code
5okl
Structure name
human afamin monoclinic crystal form
Structure deposition date
2017-07-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
40
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43652
Residue number A
77
Residue number B
86
Peptide name
Afamin
Ligandability
Cysteine 77 of Afamin
Cysteine 86 of Afamin
5okl A 515 A 560
A redox-regulated disulphide may form within Afamin between cysteines 536 and 581 (515 and 560 respectively in this structure).
Details
Redox score ?
87
PDB code
5okl
Structure name
human afamin monoclinic crystal form
Structure deposition date
2017-07-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43652
Residue number A
536
Residue number B
581
Peptide name
Afamin
Ligandability
Cysteine 536 of Afamin
Cysteine 581 of Afamin
6rq7 B 395 B 441
A redox-regulated disulphide may form within Afamin between cysteines 416 and 462 (395 and 441 respectively in this structure).
Details
Redox score ?
86
PDB code
6rq7
Structure name
gadolinium mri contrast compound binding in human plasma glycoprotein afamin - resurrection of highly anisotropic data
Structure deposition date
2019-05-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43652
Residue number A
416
Residue number B
462
Peptide name
Afamin
Ligandability
Cysteine 416 of Afamin
Cysteine 462 of Afamin
5okl A 559 A 568
A redox-regulated disulphide may form within Afamin between cysteines 580 and 589 (559 and 568 respectively in this structure).
Details
Redox score ?
85
PDB code
5okl
Structure name
human afamin monoclinic crystal form
Structure deposition date
2017-07-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43652
Residue number A
580
Residue number B
589
Peptide name
Afamin
Ligandability
Cysteine 580 of Afamin
Cysteine 589 of Afamin
6rq7 B 281 B 292
A redox-regulated disulphide may form within Afamin between cysteines 302 and 313 (281 and 292 respectively in this structure).
Details
Redox score ?
84
PDB code
6rq7
Structure name
gadolinium mri contrast compound binding in human plasma glycoprotein afamin - resurrection of highly anisotropic data
Structure deposition date
2019-05-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43652
Residue number A
302
Residue number B
313
Peptide name
Afamin
Ligandability
Cysteine 302 of Afamin
Cysteine 313 of Afamin
5okl B 363 B 372
A redox-regulated disulphide may form within Afamin between cysteines 384 and 393 (363 and 372 respectively in this structure).
Details
Redox score ?
84
PDB code
5okl
Structure name
human afamin monoclinic crystal form
Structure deposition date
2017-07-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43652
Residue number A
384
Residue number B
393
Peptide name
Afamin
Ligandability
Cysteine 384 of Afamin
Cysteine 393 of Afamin
6rq7 B 268 B 282
A redox-regulated disulphide may form within Afamin between cysteines 289 and 303 (268 and 282 respectively in this structure).
Details
Redox score ?
84
PDB code
6rq7
Structure name
gadolinium mri contrast compound binding in human plasma glycoprotein afamin - resurrection of highly anisotropic data
Structure deposition date
2019-05-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43652
Residue number A
289
Residue number B
303
Peptide name
Afamin
Ligandability
Cysteine 289 of Afamin
Cysteine 303 of Afamin
5okl B 78 B 93
A redox-regulated disulphide may form within Afamin between cysteines 99 and 114 (78 and 93 respectively in this structure).
Details
Redox score ?
84
PDB code
5okl
Structure name
human afamin monoclinic crystal form
Structure deposition date
2017-07-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43652
Residue number A
99
Residue number B
114
Peptide name
Afamin
Ligandability
Cysteine 99 of Afamin
Cysteine 114 of Afamin
6fak A 127 A 172
A redox-regulated disulphide may form within Afamin between cysteines 148 and 193 (127 and 172 respectively in this structure).
Details
Redox score ?
84
PDB code
6fak
Structure name
human afamin orthorhombic crystal form by controlled hydration
Structure deposition date
2017-12-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43652
Residue number A
148
Residue number B
193
Peptide name
Afamin
Ligandability
Cysteine 148 of Afamin
Cysteine 193 of Afamin
6fak A 319 A 364
A redox-regulated disulphide may form within Afamin between cysteines 340 and 385 (319 and 364 respectively in this structure).
Details
Redox score ?
84
PDB code
6fak
Structure name
human afamin orthorhombic crystal form by controlled hydration
Structure deposition date
2017-12-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43652
Residue number A
340
Residue number B
385
Peptide name
Afamin
Ligandability
Cysteine 340 of Afamin
Cysteine 385 of Afamin
6rq7 B 477 B 488
A redox-regulated disulphide may form within Afamin between cysteines 498 and 509 (477 and 488 respectively in this structure).
Details
Redox score ?
83
PDB code
6rq7
Structure name
gadolinium mri contrast compound binding in human plasma glycoprotein afamin - resurrection of highly anisotropic data
Structure deposition date
2019-05-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43652
Residue number A
498
Residue number B
509
Peptide name
Afamin
Ligandability
Cysteine 498 of Afamin
Cysteine 509 of Afamin
6rq7 B 92 B 103
A redox-regulated disulphide may form within Afamin between cysteines 113 and 124 (92 and 103 respectively in this structure).
Details
Redox score ?
82
PDB code
6rq7
Structure name
gadolinium mri contrast compound binding in human plasma glycoprotein afamin - resurrection of highly anisotropic data
Structure deposition date
2019-05-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43652
Residue number A
113
Residue number B
124
Peptide name
Afamin
Ligandability
Cysteine 113 of Afamin
Cysteine 124 of Afamin
6rq7 B 248 B 256
A redox-regulated disulphide may form within Afamin between cysteines 269 and 277 (248 and 256 respectively in this structure).
Details
Redox score ?
82
PDB code
6rq7
Structure name
gadolinium mri contrast compound binding in human plasma glycoprotein afamin - resurrection of highly anisotropic data
Structure deposition date
2019-05-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43652
Residue number A
269
Residue number B
277
Peptide name
Afamin
Ligandability
Cysteine 269 of Afamin
Cysteine 277 of Afamin
5okl B 462 B 478
A redox-regulated disulphide may form within Afamin between cysteines 483 and 499 (462 and 478 respectively in this structure).
Details
Redox score ?
82
PDB code
5okl
Structure name
human afamin monoclinic crystal form
Structure deposition date
2017-07-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43652
Residue number A
483
Residue number B
499
Peptide name
Afamin
Ligandability
Cysteine 483 of Afamin
Cysteine 499 of Afamin
5okl A 440 A 449
A redox-regulated disulphide may form within Afamin between cysteines 461 and 470 (440 and 449 respectively in this structure).
Details
Redox score ?
81
PDB code
5okl
Structure name
human afamin monoclinic crystal form
Structure deposition date
2017-07-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43652
Residue number A
461
Residue number B
470
Peptide name
Afamin
Ligandability
Cysteine 461 of Afamin
Cysteine 470 of Afamin
6rq7 B 203 B 249
A redox-regulated disulphide may form within Afamin between cysteines 224 and 270 (203 and 249 respectively in this structure).
Details
Redox score ?
78
PDB code
6rq7
Structure name
gadolinium mri contrast compound binding in human plasma glycoprotein afamin - resurrection of highly anisotropic data
Structure deposition date
2019-05-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43652
Residue number A
224
Residue number B
270
Peptide name
Afamin
Ligandability
Cysteine 224 of Afamin
Cysteine 270 of Afamin
5okl A 171 A 172
A redox-regulated disulphide may form within Afamin between cysteines 192 and 193 (171 and 172 respectively in this structure).
Details
Redox score ?
64
PDB code
5okl
Structure name
human afamin monoclinic crystal form
Structure deposition date
2017-07-25
Thiol separation (Å)
7
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
nan
Peptide accession
P43652
Residue number A
192
Residue number B
193
Peptide name
Afamin
Ligandability
Cysteine 192 of Afamin
Cysteine 193 of Afamin
5okl A 281 A 282
A redox-regulated disulphide may form within Afamin between cysteines 302 and 303 (281 and 282 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
59
PDB code
5okl
Structure name
human afamin monoclinic crystal form
Structure deposition date
2017-07-25
Thiol separation (Å)
6
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43652
Residue number A
302
Residue number B
303
Peptide name
Afamin
Ligandability
Cysteine 302 of Afamin
Cysteine 303 of Afamin
6fak A 363 A 364
A redox-regulated disulphide may form within Afamin between cysteines 384 and 385 (363 and 364 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
58
PDB code
6fak
Structure name
human afamin orthorhombic crystal form by controlled hydration
Structure deposition date
2017-12-15
Thiol separation (Å)
7
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43652
Residue number A
384
Residue number B
385
Peptide name
Afamin
Ligandability
Cysteine 384 of Afamin
Cysteine 385 of Afamin
5okl B 440 B 441
A redox-regulated disulphide may form within Afamin between cysteines 461 and 462 (440 and 441 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
57
PDB code
5okl
Structure name
human afamin monoclinic crystal form
Structure deposition date
2017-07-25
Thiol separation (Å)
7
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43652
Residue number A
461
Residue number B
462
Peptide name
Afamin
Ligandability
Cysteine 461 of Afamin
Cysteine 462 of Afamin
5okl B 92 B 93
A redox-regulated disulphide may form within Afamin between cysteines 113 and 114 (92 and 93 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
5okl
Structure name
human afamin monoclinic crystal form
Structure deposition date
2017-07-25
Thiol separation (Å)
7
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43652
Residue number A
113
Residue number B
114
Peptide name
Afamin
Ligandability
Cysteine 113 of Afamin
Cysteine 114 of Afamin
6rq7 B 477 B 478
A redox-regulated disulphide may form within Afamin between cysteines 498 and 499 (477 and 478 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
6rq7
Structure name
gadolinium mri contrast compound binding in human plasma glycoprotein afamin - resurrection of highly anisotropic data
Structure deposition date
2019-05-15
Thiol separation (Å)
7
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43652
Residue number A
498
Residue number B
499
Peptide name
Afamin
Ligandability
Cysteine 498 of Afamin
Cysteine 499 of Afamin
5okl B 319 B 363
A redox-regulated disulphide may form within Afamin between cysteines 340 and 384 (319 and 363 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
5okl
Structure name
human afamin monoclinic crystal form
Structure deposition date
2017-07-25
Thiol separation (Å)
7
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43652
Residue number A
340
Residue number B
384
Peptide name
Afamin
Ligandability
Cysteine 340 of Afamin
Cysteine 384 of Afamin
5okl A 248 A 249
A redox-regulated disulphide may form within Afamin between cysteines 269 and 270 (248 and 249 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
5okl
Structure name
human afamin monoclinic crystal form
Structure deposition date
2017-07-25
Thiol separation (Å)
7
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43652
Residue number A
269
Residue number B
270
Peptide name
Afamin
Ligandability
Cysteine 269 of Afamin
Cysteine 270 of Afamin
5okl A 559 A 560
A redox-regulated disulphide may form within Afamin between cysteines 580 and 581 (559 and 560 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
54
PDB code
5okl
Structure name
human afamin monoclinic crystal form
Structure deposition date
2017-07-25
Thiol separation (Å)
7
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43652
Residue number A
580
Residue number B
581
Peptide name
Afamin
Ligandability
Cysteine 580 of Afamin
Cysteine 581 of Afamin
5okl B 268 B 281
A redox-regulated disulphide may form within Afamin between cysteines 289 and 302 (268 and 281 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
54
PDB code
5okl
Structure name
human afamin monoclinic crystal form
Structure deposition date
2017-07-25
Thiol separation (Å)
7
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43652
Residue number A
289
Residue number B
302
Peptide name
Afamin
Ligandability
Cysteine 289 of Afamin
Cysteine 302 of Afamin
6fak A 78 A 92
A redox-regulated disulphide may form within Afamin between cysteines 99 and 113 (78 and 92 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
6fak
Structure name
human afamin orthorhombic crystal form by controlled hydration
Structure deposition date
2017-12-15
Thiol separation (Å)
7
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43652
Residue number A
99
Residue number B
113
Peptide name
Afamin
Ligandability
Cysteine 99 of Afamin
Cysteine 113 of Afamin
6fak A 515 A 559
A redox-regulated disulphide may form within Afamin between cysteines 536 and 580 (515 and 559 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
6fak
Structure name
human afamin orthorhombic crystal form by controlled hydration
Structure deposition date
2017-12-15
Thiol separation (Å)
8
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43652
Residue number A
536
Residue number B
580
Peptide name
Afamin
Ligandability
Cysteine 536 of Afamin
Cysteine 580 of Afamin
5okl B 395 B 440
A redox-regulated disulphide may form within Afamin between cysteines 416 and 461 (395 and 440 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
5okl
Structure name
human afamin monoclinic crystal form
Structure deposition date
2017-07-25
Thiol separation (Å)
7
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43652
Residue number A
416
Residue number B
461
Peptide name
Afamin
Ligandability
Cysteine 416 of Afamin
Cysteine 461 of Afamin
5okl B 364 B 372
A redox-regulated disulphide may form within Afamin between cysteines 385 and 393 (364 and 372 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
5okl
Structure name
human afamin monoclinic crystal form
Structure deposition date
2017-07-25
Thiol separation (Å)
8
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43652
Residue number A
385
Residue number B
393
Peptide name
Afamin
Ligandability
Cysteine 385 of Afamin
Cysteine 393 of Afamin
6fak A 127 A 171
A redox-regulated disulphide may form within Afamin between cysteines 148 and 192 (127 and 171 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
6fak
Structure name
human afamin orthorhombic crystal form by controlled hydration
Structure deposition date
2017-12-15
Thiol separation (Å)
8
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43652
Residue number A
148
Residue number B
192
Peptide name
Afamin
Ligandability
Cysteine 148 of Afamin
Cysteine 192 of Afamin
6rq7 B 462 B 477
A redox-regulated disulphide may form within Afamin between cysteines 483 and 498 (462 and 477 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
6rq7
Structure name
gadolinium mri contrast compound binding in human plasma glycoprotein afamin - resurrection of highly anisotropic data
Structure deposition date
2019-05-15
Thiol separation (Å)
8
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43652
Residue number A
483
Residue number B
498
Peptide name
Afamin
Ligandability
Cysteine 483 of Afamin
Cysteine 498 of Afamin
6fak A 172 A 180
A redox-regulated disulphide may form within Afamin between cysteines 193 and 201 (172 and 180 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
6fak
Structure name
human afamin orthorhombic crystal form by controlled hydration
Structure deposition date
2017-12-15
Thiol separation (Å)
8
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43652
Residue number A
193
Residue number B
201
Peptide name
Afamin
Ligandability
Cysteine 193 of Afamin
Cysteine 201 of Afamin
5okl A 203 A 248
A redox-regulated disulphide may form within Afamin between cysteines 224 and 269 (203 and 248 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
5okl
Structure name
human afamin monoclinic crystal form
Structure deposition date
2017-07-25
Thiol separation (Å)
7
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43652
Residue number A
224
Residue number B
269
Peptide name
Afamin
Ligandability
Cysteine 224 of Afamin
Cysteine 269 of Afamin
6rq7 B 93 B 103
A redox-regulated disulphide may form within Afamin between cysteines 114 and 124 (93 and 103 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
6rq7
Structure name
gadolinium mri contrast compound binding in human plasma glycoprotein afamin - resurrection of highly anisotropic data
Structure deposition date
2019-05-15
Thiol separation (Å)
8
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43652
Residue number A
114
Residue number B
124
Peptide name
Afamin
Ligandability
Cysteine 114 of Afamin
Cysteine 124 of Afamin
6fak A 515 A 568
A redox-regulated disulphide may form within Afamin between cysteines 536 and 589 (515 and 568 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
6fak
Structure name
human afamin orthorhombic crystal form by controlled hydration
Structure deposition date
2017-12-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43652
Residue number A
536
Residue number B
589
Peptide name
Afamin
Ligandability
Cysteine 536 of Afamin
Cysteine 589 of Afamin
5okl B 478 B 488
A redox-regulated disulphide may form within Afamin between cysteines 499 and 509 (478 and 488 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
5okl
Structure name
human afamin monoclinic crystal form
Structure deposition date
2017-07-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43652
Residue number A
499
Residue number B
509
Peptide name
Afamin
Ligandability
Cysteine 499 of Afamin
Cysteine 509 of Afamin
6fak A 127 A 180
A redox-regulated disulphide may form within Afamin between cysteines 148 and 201 (127 and 180 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
6fak
Structure name
human afamin orthorhombic crystal form by controlled hydration
Structure deposition date
2017-12-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43652
Residue number A
148
Residue number B
201
Peptide name
Afamin
Ligandability
Cysteine 148 of Afamin
Cysteine 201 of Afamin
6fak A 560 A 568
A redox-regulated disulphide may form within Afamin between cysteines 581 and 589 (560 and 568 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
6fak
Structure name
human afamin orthorhombic crystal form by controlled hydration
Structure deposition date
2017-12-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
P43652
Residue number A
581
Residue number B
589
Peptide name
Afamin
Ligandability
Cysteine 581 of Afamin
Cysteine 589 of Afamin
If this tool was useful for finding a disulphide, please cite: